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Conserved domains on  [gi|15225693|ref|NP_180811|]
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alpha/beta-Hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

dienelactone hydrolase family protein( domain architecture ID 11123939)

dienelactone hydrolase family protein such as carboxymethylenebutenolidase, which catalyzes the reaction between 4-carboxymethylenebut-2-en-4-olide and water to produce 4-oxohex-2-enedioate

CATH:  3.40.50.1820
EC:  3.-.-.-|3.1.-.-
Gene Ontology:  GO:0005829|GO:0016787
PubMed:  2380986|19508187|12369917

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
19-236 1.38e-74

Dienelactone hydrolase family;


:

Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 225.31  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    19 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 91
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    92 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 166
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   167 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 236
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
19-236 1.38e-74

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 225.31  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    19 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 91
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    92 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 166
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   167 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 236
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-235 9.81e-53

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 170.15  E-value: 9.81e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   7 RKIQIQ-RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKISQLepGFKALIPDLY-RGKVGLDTAEAQHLM 81
Cdd:COG0412   4 ETVTIPtPDGVTLPGYLArpaGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA--GYVVLAPDLYgRGGPGDDPDEARALM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  82 DGLDWPGAIKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYGTPSSE--LADPAQAKAPIQA 156
Cdd:COG0412  82 GALDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADdlLDLAARIKAPVLL 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225693 157 HFGELDNFVGFSDVTAaknLEEKLKASGVAHEVHIYPGNGHAFLNRspegvsrrksmGLSDEDEAAVELAWSRFTSWMK 235
Cdd:COG0412 162 LYGEKDPLVPPEQVAA---LEAALAAAGVDVELHVYPGAGHGFTNP-----------GRPRYDPAAAEDAWQRTLAFLA 226
 
Name Accession Description Interval E-value
DLH pfam01738
Dienelactone hydrolase family;
19-236 1.38e-74

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 225.31  E-value: 1.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    19 DAYVVGKDDA--PGIVVIQEWWGVDfeiKNHA-IKISQLEPGFKALIPDLYRGKVG-LDTAEAQHLMDGLDWPGAIK--- 91
Cdd:pfam01738   1 DAYLATPKNPpwPVVVVFQEIFGVN---DNIReIADRLADEGYVALAPDLYFRQGDpNDEADAARAMFELVSKRVMEkvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693    92 -DIRASVNWLKSN---GSKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYG-TPSSELADPAQAKAPIQAHFGELDNFVG 166
Cdd:pfam01738  78 dDLEAAVNYLKSQpevSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGvGPEPPLIEAPDIKAPILFHFGEEDHFVP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   167 FSDVtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGvsrrksmglsdEDEAAVELAWSRFTSWMKQ 236
Cdd:pfam01738 158 ADSR---ELIEEALKAANVDHQIHSYPGAGHAFANDSRPS-----------YNAAAAEDAWERTLEFFKQ 213
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-235 9.81e-53

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 170.15  E-value: 9.81e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   7 RKIQIQ-RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKISQLepGFKALIPDLY-RGKVGLDTAEAQHLM 81
Cdd:COG0412   4 ETVTIPtPDGVTLPGYLArpaGGGPRPGVVVLHEIFGLNPHIRDVARRLAAA--GYVVLAPDLYgRGGPGDDPDEARALM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  82 DGLDWPGAIKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPEVDAVVGFYGTPSSE--LADPAQAKAPIQA 156
Cdd:COG0412  82 GALDPELLAADLRAALDWLKAQPevdAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADdlLDLAARIKAPVLL 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225693 157 HFGELDNFVGFSDVTAaknLEEKLKASGVAHEVHIYPGNGHAFLNRspegvsrrksmGLSDEDEAAVELAWSRFTSWMK 235
Cdd:COG0412 162 LYGEKDPLVPPEQVAA---LEAALAAAGVDVELHVYPGAGHGFTNP-----------GRPRYDPAAAEDAWQRTLAFLA 226
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
86-239 1.02e-13

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 67.59  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  86 WPGAIKDIRASVNWLKSNGSK------KVGVTGMCMGGALAIASSVL-----VPEVDAVVGFYGtPSSELADPAQAK--- 151
Cdd:COG0657  60 FPAALEDAYAALRWLRANAAElgidpdRIAVAGDSAGGHLAAALALRardrgGPRPAAQVLIYP-VLDLTASPLRADlag 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693 152 -APIQAHFGELDNFVGFSdvtaaKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGVSRRksmglsdedeaavelAWSRF 230
Cdd:COG0657 139 lPPTLIVTGEADPLVDES-----EALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARA---------------ALAEI 198


                ....*....
gi 15225693 231 TSWMKQYLA 239
Cdd:COG0657 199 AAFLRRALA 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
13-210 2.90e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.41  E-value: 2.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  13 RDDTTFDAYVV---GKDDAPGIVVIQEWWGVDFEIKNHAIKisQL-EPGFKALIPDlYRGkvgldtaeaqHLMDGLDWPG 88
Cdd:COG1506   5 ADGTTLPGWLYlpaDGKKYPVVVYVHGGPGSRDDSFLPLAQ--ALaSRGYAVLAPD-YRG----------YGESAGDWGG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  89 A-IKDIRASVNWLKSNG---SKKVGVTGMCMGGALAIASSVLVPE-VDAVV--------------------GFYGTPSSE 143
Cdd:COG1506  72 DeVDDVLAAIDYLAARPyvdPDRIGIYGHSYGGYMALLAAARHPDrFKAAValagvsdlrsyygttreyteRLMGGPWED 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225693 144 LADPAQA---------KAPIQAHFGELDNFVGFSDvtaAKNLEEKLKASGVAHEVHIYPGNGHAFLNRSPEGVSRR 210
Cdd:COG1506 152 PEAYAARsplayadklKTPLLLIHGEADDRVPPEQ---AERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLER 224
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
54-201 1.94e-05

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 44.22  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  54 LEPGFKALIPDLyRGkVGLDTAEAQHLmdgLDWPGAIKDIRASVNWLKSNGSKKVGVTGMCMGGALA----------IAS 123
Cdd:COG2267  52 AAAGYAVLAFDL-RG-HGRSDGPRGHV---DSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIAllyaarypdrVAG 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693 124 SVLV-------PEVDAVVGFYGtpSSELADPAQA-KAPIQAHFGELDNFVgfsDVTAAKNLEEKLKASGvahEVHIYPGN 195
Cdd:COG2267 127 LVLLapayradPLLGPSARWLR--ALRLAEALARiDVPVLVLHGGADRVV---PPEAARRLAARLSPDV---ELVLLPGA 198


                ....*.
gi 15225693 196 GHAFLN 201
Cdd:COG2267 199 RHELLN 204
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 86-138 6.79e-05

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 42.55  E-value: 6.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225693    86 WPGAIKDIRASVNWLKSNGSK------KVGVTGMCMGGALA--------------------IASSVLVPEVDAVVGFYG 138
Cdd:pfam20434  63 FPAQIQDVKAAIRFLRANAAKygidtnKIALMGFSAGGHLAllaglsnnnkefegnvgdytPESSKESFKVNAVVDFYG 141
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 57-134 3.39e-04

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 40.67  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693  57 GFKALIPDlYRGkvgldTAEAQHLMDGLDWPgAIKDIRASVNWLKS---NGSKKVGVTGMCMGGALAIASSVLVPEVDAV 133
Cdd:COG1073  64 GFNVLAFD-YRG-----YGESEGEPREEGSP-ERRDARAAVDYLRTlpgVDPERIGLLGISLGGGYALNAAATDPRVKAV 136


                .
gi 15225693 134 V 134
Cdd:COG1073 137 I 137
YpfH COG0400
Predicted esterase [General function prediction only];
116-198 3.68e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 40.28  E-value: 3.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693 116 GGALAIASSVLVPE-VDAVVGFYGT----PSSELADPAQAKAPI-QAHfGELDNFVgfsDVTAAKNLEEKLKASGVAHEV 189
Cdd:COG0400  99 GAAMALSLALRRPElLAGVVALSGYlpgeEALPAPEAALAGTPVfLAH-GTQDPVI---PVERAREAAEALEAAGADVTY 174


                ....*....
gi 15225693 190 HIYPGnGHA 198
Cdd:COG0400 175 REYPG-GHE 182
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
 104-203 4.02e-04

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 40.44  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225693   104 GSKKVGVTGMCMGGALAIASSVLVP-EVDAVVGFYGT--PSSELADPAQA---KAPI-QAHfGELDNFVgfsDVTAAKNL 176
Cdd:pfam02230 103 PSSRIIIGGFSQGAMLALYSALTLPlPLGGIVAFSGFlpLPTKFPSHPNLvtkKTPIfLIH-GEEDPVV---PLALGKLA 178

                          90       100
                  ....*....|....*....|....*..
gi 15225693   177 EEKLKASGVAHEVHIYPGNGHAFLNRS 203
Cdd:pfam02230 179 KEYLKTSLNKVELKIYEGLAHSICGRE 205
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
85-160 6.78e-04

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.92  E-value: 6.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225693  85 DWpgaIKDIRASVNWLKSNGsKKVGVTGMCMGGALAIASSVLVPEVDAVVgFYGtPSSELADPAQAKAPIQAHFGE 160
Cdd:COG1647  67 DW---LEDVEEAYEILKAGY-DKVIVIGLSMGGLLALLLAARYPDVAGLV-LLS-PALKIDDPSAPLLPLLKYLAR 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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